SitesBLAST
Comparing WP_022047120.1 NCBI__GCF_001406815.1:WP_022047120.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
2f2aA Structure of tRNA-dependent amidotransferase gatcab complexed with gln (see paper)
54% identity, 97% coverage: 2:474/487 of query aligns to 10:473/485 of 2f2aA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding glutamine: G130 (= G130), S154 (= S154), D174 (= D174), T175 (= T175), G176 (= G176), S178 (= S178), F206 (≠ Y206), Y309 (= Y309), Y310 (= Y310), R358 (= R358), D425 (= D425)
2dqnA Structure of tRNA-dependent amidotransferase gatcab complexed with asn (see paper)
54% identity, 97% coverage: 2:474/487 of query aligns to 10:473/485 of 2dqnA
- active site: K79 (= K79), S154 (= S154), S155 (= S155), S173 (= S173), T175 (= T175), G176 (= G176), G177 (= G177), S178 (= S178), Q181 (= Q181)
- binding asparagine: M129 (= M129), G130 (= G130), T175 (= T175), G176 (= G176), S178 (= S178), Y309 (= Y309), Y310 (= Y310), R358 (= R358), D425 (= D425)
3h0mA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 97% coverage: 10:483/487 of query aligns to 9:476/478 of 3h0mA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding glutamine: M122 (= M129), G123 (= G130), D167 (= D174), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), F199 (≠ Y206), Y302 (= Y309), R351 (= R358), D418 (= D425)
3h0lA Structure of tRNA-dependent amidotransferase gatcab from aquifex aeolicus (see paper)
51% identity, 97% coverage: 10:483/487 of query aligns to 9:476/478 of 3h0lA
- active site: K72 (= K79), S147 (= S154), S148 (= S155), S166 (= S173), T168 (= T175), G169 (= G176), G170 (= G177), S171 (= S178), Q174 (= Q181)
- binding asparagine: G123 (= G130), S147 (= S154), G169 (= G176), G170 (= G177), S171 (= S178), Y302 (= Y309), R351 (= R358), D418 (= D425)
3kfuE Crystal structure of the transamidosome (see paper)
45% identity, 97% coverage: 8:481/487 of query aligns to 2:461/468 of 3kfuE
4n0iA Crystal structure of s. Cerevisiae mitochondrial gatfab in complex with glutamine (see paper)
37% identity, 81% coverage: 66:458/487 of query aligns to 29:434/450 of 4n0iA
- active site: K38 (= K79), S116 (= S154), S117 (= S155), T135 (≠ S173), T137 (= T175), G138 (= G176), G139 (= G177), S140 (= S178), L143 (≠ Q181)
- binding glutamine: G89 (= G130), T137 (= T175), G138 (= G176), S140 (= S178), Y168 (= Y206), Y271 (= Y309), Y272 (= Y310), R320 (= R358), D404 (= D425)
3a1iA Crystal structure of rhodococcus sp. N-771 amidase complexed with benzamide (see paper)
33% identity, 86% coverage: 66:484/487 of query aligns to 82:507/508 of 3a1iA
- active site: K95 (= K79), S170 (= S154), S171 (= S155), G189 (≠ S173), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), I197 (≠ Q181)
- binding benzamide: F145 (≠ M129), S146 (≠ G130), G147 (≠ S131), Q191 (≠ T175), G192 (= G176), G193 (= G177), A194 (≠ S178), W327 (≠ Y309)
6c6gA An unexpected vestigial protein complex reveals the evolutionary origins of an s-triazine catabolic enzyme. Inhibitor bound complex. (see paper)
32% identity, 97% coverage: 6:476/487 of query aligns to 1:450/457 of 6c6gA
1m21A Crystal structure analysis of the peptide amidase pam in complex with the competitive inhibitor chymostatin (see paper)
32% identity, 85% coverage: 70:483/487 of query aligns to 72:484/487 of 1m21A
- active site: K81 (= K79), S160 (= S154), S161 (= S155), T179 (≠ S173), T181 (= T175), D182 (≠ G176), G183 (= G177), S184 (= S178), C187 (≠ Q181)
- binding : A129 (= A128), N130 (≠ M129), F131 (vs. gap), C158 (≠ G152), G159 (= G153), S160 (= S154), S184 (= S178), C187 (≠ Q181), I212 (≠ Y206), R318 (≠ Y310), L321 (≠ A313), L365 (≠ M360), F426 (≠ D417)
6diiH Structure of arabidopsis fatty acid amide hydrolase in complex with methyl linolenyl fluorophosphonate (see paper)
27% identity, 91% coverage: 43:484/487 of query aligns to 169:598/616 of 6diiH
- binding methyl-9Z,12Z,15Z-octadecatrienylphosphonofluoridate: G255 (≠ A128), T258 (≠ S131), S281 (= S154), G302 (≠ T175), G303 (= G176), S305 (= S178), S472 (= S363), I532 (≠ V426), M539 (vs. gap)
Sites not aligning to the query:
Q7XJJ7 Fatty acid amide hydrolase; AtFAAH; N-acylethanolamine amidohydrolase; EC 3.5.1.99 from Arabidopsis thaliana (Mouse-ear cress) (see 2 papers)
27% identity, 91% coverage: 43:484/487 of query aligns to 169:598/607 of Q7XJJ7
- K205 (= K79) mutation to A: Loss of activity.
- SS 281:282 (= SS 154:155) mutation to AA: Loss of activity.
- GGGS 302:305 (≠ TGGS 175:178) binding substrate
- S305 (= S178) mutation to A: Loss of activity.
- R307 (= R180) mutation to A: Loss of activity.
- S360 (≠ Y233) mutation to A: No effect.
8ey9B Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with 9-hydroxy-10,12-octadecadienoyl-ethanolamide
27% identity, 91% coverage: 43:484/487 of query aligns to 169:598/605 of 8ey9B
- binding (9R,10E,12Z)-9-hydroxy-N-(2-hydroxyethyl)octadeca-10,12-dienamide: G255 (≠ A128), G302 (≠ T175), G303 (= G176), G304 (= G177), A305 (≠ S178), V442 (≠ Y310), I475 (≠ L366), M539 (vs. gap)
Sites not aligning to the query:
8ey1D Structure of arabidopsis fatty acid amide hydrolase mutant s305a in complex with n-(3-oxododecanoyl)-l-homoserine lactone
27% identity, 91% coverage: 43:484/487 of query aligns to 169:598/605 of 8ey1D
5h6sC Crystal structure of hydrazidase s179a mutant complexed with a substrate (see paper)
26% identity, 97% coverage: 6:475/487 of query aligns to 5:445/457 of 5h6sC
- active site: K77 (= K79), S152 (= S154), S153 (= S155), L173 (≠ T175), G174 (= G176), G175 (= G177), S176 (= S178)
- binding 4-oxidanylbenzohydrazide: C126 (≠ A128), R128 (≠ G130), W129 (≠ S131), S152 (= S154), L173 (≠ T175), G174 (= G176), S176 (= S178), W306 (≠ Y309), F338 (≠ Y371)
Q84DC4 Mandelamide hydrolase; EC 3.5.1.86 from Pseudomonas putida (Arthrobacter siderocapsulatus) (see 2 papers)
29% identity, 94% coverage: 2:458/487 of query aligns to 24:471/507 of Q84DC4
- T31 (≠ V9) mutation to I: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with N-437.
- K100 (= K79) mutation to A: Abolishes activity on mandelamide.
- S180 (= S154) mutation to A: Significantly decreases activity on mandelamide.
- S181 (= S155) mutation to A: Significantly decreases activity on mandelamide.
- G202 (= G176) mutation to A: Increase in KM values for aromatic substrates, but not aliphatic substrates. Active against lactamide but not against mandelamide; when associated with H-207 and E-382.; mutation to V: Increase in KM values for aromatic substrates, but not aliphatic substrates.
- S204 (= S178) mutation to A: Abolishes activity on mandelamide.
- Q207 (= Q181) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with E-382. Active against lactamide but not against mandelamide; when associated with A-202 and E-382. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with S-316 and N-437.
- S316 (≠ A305) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-437.
- Q382 (≠ S368) mutation to H: Increases activity on lactamide, does not affect activity on mandelamide; when associated with H-207. Active against lactamide but not against mandelamide; when associated with A-202 and H-207.
- I437 (≠ S430) mutation to N: More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with I-31. More active on the (S)-enantiomers of mandelamide and lactamide than the (R)-enantiomers; when associated with H-207 and N-316.
Q936X2 Allophanate hydrolase; EC 3.5.1.54 from Pseudomonas sp. (strain ADP) (see paper)
31% identity, 87% coverage: 49:473/487 of query aligns to 62:460/605 of Q936X2
- K91 (= K79) mutation to A: Loss of activity.
- S165 (= S154) mutation to A: Loss of activity.
- S189 (= S178) mutation to A: Loss of activity.
1o9oA Crystal structure of the s131a mutant of malonamidase e2 complexed with malonamate from bradyrhizobium japonicum (see paper)
29% identity, 96% coverage: 6:474/487 of query aligns to 2:407/412 of 1o9oA
- active site: K62 (= K79), A131 (≠ S154), S132 (= S155), T150 (≠ S173), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181)
- binding 3-amino-3-oxopropanoic acid: G130 (= G153), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181), P359 (= P418)
4yjiA The crystal structure of a bacterial aryl acylamidase belonging to the amidase signature (as) enzymes family (see paper)
28% identity, 98% coverage: 7:481/487 of query aligns to 7:480/490 of 4yjiA
- active site: K79 (= K79), S158 (= S154), S159 (= S155), G179 (≠ T175), G180 (= G176), G181 (= G177), A182 (≠ S178)
- binding n-(4-hydroxyphenyl)acetamide (tylenol): L81 (≠ N81), G132 (≠ A128), S158 (= S154), G179 (≠ T175), G180 (= G176), A182 (≠ S178)
1ocmA The crystal structure of malonamidase e2 covalently complexed with pyrophosphate from bradyrhizobium japonicum (see paper)
29% identity, 96% coverage: 6:474/487 of query aligns to 2:407/412 of 1ocmA
- active site: K62 (= K79), S131 (= S154), S132 (= S155), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178)
- binding pyrophosphate 2-: R113 (≠ G130), S131 (= S154), Q151 (≠ D174), T152 (= T175), G153 (= G176), G154 (= G177), S155 (= S178), R158 (≠ Q181), P359 (= P418)
4gysB Granulibacter bethesdensis allophanate hydrolase co-crystallized with malonate (see paper)
30% identity, 84% coverage: 60:466/487 of query aligns to 52:430/461 of 4gysB
- active site: K72 (= K79), S146 (= S154), S147 (= S155), T165 (≠ S173), T167 (= T175), A168 (≠ G176), G169 (= G177), S170 (= S178), V173 (≠ Q181)
- binding malonate ion: A120 (= A128), G122 (= G130), S146 (= S154), T167 (= T175), A168 (≠ G176), S170 (= S178), S193 (≠ Y201), G194 (= G202), V195 (≠ L203), R200 (≠ S208), Y297 (= Y329), R305 (≠ E335)
Query Sequence
>WP_022047120.1 NCBI__GCF_001406815.1:WP_022047120.1
MNLLSLTAVELGKKIKAHEVTVEEATRAALDAIRAKEKDINSFVTVDEESAMIRAKEVQK
MIDDGTLTGPLAGVPVAIKDNMCTKGMLTTCSSKILYNFIPTYTAEAVINLEKAGAVILG
KTNMDEFAMGSTTETSAYGETKNPWNTAHVPGGSSGGSCAAVAAEECYYALGSDTGGSIR
QPSSFCGVTGIKPTYGTVSRYGLIAYGSSLDQIGPIAKDVTDCATILETITSYDKKDSTS
VKREETDFTSALVDDVKGMKIGIPRDYLGEGLDPEVKEAILAAAKTLEEKGAIVEEFDLS
LVEYAIPAYYVIAAAEASSNLARFDGVKYGYRTKEYEGLHNMYKKSRSEGFGPEVKRRIM
LGSFVLSSGYYDAYYLKALRTKALIKQAFDKAFAKYDVILGPAAPTTAPKLGESLSDPLK
MYLGDVYTVSVNLAGLPGISVPCGVDSKGLPIGLQLIGDCFKEKNIIRAAYSFEQTRTYQ
HSPAAEA
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SitesBLAST's Database
SitesBLAST's database includes
(1) SwissProt
entries with experimentally-supported functional features;
and (2) protein structures with bound ligands, from the
BioLip database.
by Morgan Price,
Arkin group
Lawrence Berkeley National Laboratory